http://purl.uniprot.org/citations/7487879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/7487879 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/7487879 | http://www.w3.org/2000/01/rdf-schema#comment | "Reactions of oestrogens and androgens at position C-17 are catalysed by 17 beta-hydroxysteroid dehydrogenases (17 beta-HSDs). Cloning of the cDNA of a novel human 17 beta-HSD IV and expression of its mRNA are described. A probe derived from the recently discovered porcine 17 beta-oestradiol dehydrogenase (17 beta-EDH) was used to isolate a 2.6 kb human cDNA encoding a continuous protein of 736 amino acids of high (84%) similarity to the porcine 17 beta-EDH. The calculated molecular mass of the human enzyme is 79,595 Da. Other sequence similarities shared by the two enzymes are: an N-terminal sequence which is similar to that of members of the short-chain alcohol dehydrogenase family; amino acids 343-607 which are similar to the C-terminal domains of a trifunctional Candida tropicalis enzyme and the FOX2 gene product of Saccharomyces cerevisiae; amino acids 596-736 which are similar to human sterol carrier protein 2. The previously cloned human 17 beta-HSD I, II and III are less than 25% identical with 17 beta-HSD IV. mRNA for HSD IV is a single species of 3.0 kb, present in many tissues with highest concentrations in liver, heart, prostate and testes. When over-expressed in mammalian cells, the human 17 beta-HSD IV enzyme displays a specific unidirectional oxidative 17 beta-HSD activity."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3110437"xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3110437"xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "de Launoit Y."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "de Launoit Y."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Stehelin D."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Stehelin D."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Adamski J."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Adamski J."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Leenders F."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Leenders F."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Begue A."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Begue A."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Jungblut P.W."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Jungblut P.W."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Monte D."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Monte D."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Normand T."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/author | "Normand T."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
http://purl.uniprot.org/citations/7487879 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |